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BACSU:FLIY

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Species (Taxon ID) Bacillus subtilis (strain 168). (224308)
Gene Name(s) fliY (synonyms: cheD)
Protein Name(s) Flagellar motor switch phosphatase FliY

CheY-P phosphatase FliY Flagellar motor switch protein FliY

External Links
UniProt P24073
EMBL M86738
AL009126
M37691
PIR S25279
RefSeq NP_389514.1
ProteinModelPortal P24073
SMR P24073
STRING 224308.BSU16320
PaxDb P24073
EnsemblBacteria CAB13505
GeneID 936421
KEGG bsu:BSU16320
PATRIC 18975071
GenoList BSU16320
eggNOG COG1886
HOGENOM HOG000057238
InParanoid P24073
KO K02417
OMA MMGGDGK
OrthoDB EOG6Q5NX5
PhylomeDB P24073
BioCyc BSUB:BSU16320-MONOMER
Proteomes UP000001570
GO GO:0009425
GO:0005886
GO:0003774
GO:0004721
GO:0071973
GO:0006935
GO:0016311
Gene3D 3.40.1550.10
InterPro IPR007597
IPR028976
IPR012826
IPR001172
IPR001543
Pfam PF04509
PF01052
PRINTS PR00956
SUPFAM SSF101801
SSF103039
TIGRFAMs TIGR02480

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0006935

chemotaxis

PMID:12920116[1]

ECO:0000315

P

See Figure 4 and Results: N-terminal Deletions in FliM and FliY Promote Opposite Phenotypes in the Tethered Cell Assay in Vivo. FliY mutant did not match wild-type swarm diameters and did not respond to addition or removal of the attractant asparagine.

complete
CACAO 10481

GO:0004721

phosphoprotein phosphatase activity

PMID:12920116[1]

ECO:0000314

F

Figure 5 shows Fliy activity in dephosphorylation of Chey-P

complete
CACAO 2133

GO:0016311

dephosphorylation

PMID:12920116[1]

ECO:0000315

P

See Fig 5: increasing concentrations of FliY increase the speed of CheY-P dephosphorylation.

complete
CACAO 10483

GO:1902021

regulation of bacterial-type flagellum-dependent cell motility

PMID:12920116[1]

ECO:0000315

P

"See Results: N-terminal Deletions in FliM and FliY Promote Opposite Phenotypes in the Tethered Cell Assay in Vivo. Figure 4B shows that the modified FliY causes rotational direction of a tethered cell to reverse in a tethered cell assay.

complete
CACAO 10484

GO:0016311

dephosphorylation

PMID:12920116[1]

ECO:0000315

P

See Fig 5: increasing concentrations of FliY increase the speed of CheY-P dephosphorylation.

complete

GO:0071978

bacterial-type flagellum-dependent swarming motility

PMID:25313396[2]

ECO:0000315

P

Fig (4) shows that the fliY mutant of B.subtilis, a part of the fla-che operon, shows a significant decrease in in swarm radius in comparison to Wild-Type cells.

complete
CACAO 13191

involved_in

GO:1902021

regulation of bacterial-type flagellum-dependent cell motility

PMID:12920116[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

GO:0044780

bacterial-type flagellum assembly

PMID:25313396[2]

ECO:0000315

P

Figure 5 top left panel shows that FliY, a fla-che-encoded protein, is required for hook-basal body assembly in B. subtilis.

complete
CACAO 13225

involved_in

GO:0016311

dephosphorylation

PMID:12920116[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006935

chemotaxis

PMID:12920116[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004721

phosphoprotein phosphatase activity

PMID:12920116[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006470

protein dephosphorylation

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0004721

P

Seeded From UniProt

complete

enables

GO:0003774

motor activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001172

F

Seeded From UniProt

complete

involved_in

GO:0006935

chemotaxis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001172
InterPro:IPR012826

P

Seeded From UniProt

complete

part_of

GO:0009288

bacterial-type flagellum

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012826

C

Seeded From UniProt

complete

part_of

GO:0009425

bacterial-type flagellum basal body

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001172

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012826

C

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR007597

F

Seeded From UniProt

complete

involved_in

GO:0071973

bacterial-type flagellum-dependent cell motility

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001172
InterPro:IPR012826

P

Seeded From UniProt

complete

involved_in

GO:0097588

archaeal or bacterial-type flagellum-dependent cell motility

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0283

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-SubCell:SL-0039

C

Seeded From UniProt

complete

involved_in

GO:0006935

chemotaxis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0145

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 Szurmant, H et al. (2003) Bacillus subtilis hydrolyzes CheY-P at the location of its action, the flagellar switch. J. Biol. Chem. 278 48611-6 PubMed GONUTS page
  2. 2.0 2.1 Calvo, RA & Kearns, DB (2015) FlgM is secreted by the flagellar export apparatus in Bacillus subtilis. J. Bacteriol. 197 81-91 PubMed GONUTS page